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P32019

- I5P2_HUMAN

UniProt

P32019 - I5P2_HUMAN

Protein

Type II inositol 1,4,5-trisphosphate 5-phosphatase

Gene

INPP5B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 4 (15 Dec 2009)
      Previous versions | rss
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    Functioni

    Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events.1 Publication

    Catalytic activityi

    1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi355 – 3551Magnesium1 Publication
    Metal bindingi383 – 3831Magnesium1 Publication
    Binding sitei383 – 3831Substrate

    GO - Molecular functioni

    1. inositol-1,4,5-trisphosphate 5-phosphatase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. inositol phosphate metabolic process Source: Reactome
    2. in utero embryonic development Source: Ensembl
    3. phosphatidylinositol dephosphorylation Source: UniProtKB
    4. regulation of protein processing Source: Ensembl
    5. regulation of small GTPase mediated signal transduction Source: Reactome
    6. small GTPase mediated signal transduction Source: Reactome
    7. small molecule metabolic process Source: Reactome
    8. spermatogenesis Source: Ensembl
    9. sperm motility Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05898-MONOMER.
    BRENDAi3.1.3.36. 2681.
    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
    REACT_150352. Synthesis of IP2, IP, and Ins in the cytosol.
    SABIO-RKP32019.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type II inositol 1,4,5-trisphosphate 5-phosphatase (EC:3.1.3.36)
    Alternative name(s):
    75 kDa inositol polyphosphate-5-phosphatase
    Phosphoinositide 5-phosphatase
    Short name:
    5PTase
    Gene namesi
    Name:INPP5B
    Synonyms:OCRL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6077. INPP5B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. early endosome membrane Source: UniProtKB-SubCell
    4. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
    5. Golgi apparatus Source: UniProtKB-SubCell
    6. integral component of membrane Source: Ensembl
    7. membrane Source: UniProtKB
    8. microtubule cytoskeleton Source: HPA
    9. phagocytic vesicle membrane Source: UniProtKB-SubCell
    10. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi990 – 9901C → S: Loss of prenylation and membrane localization. 1 Publication

    Organism-specific databases

    PharmGKBiPA29885.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 990990Type II inositol 1,4,5-trisphosphate 5-phosphatasePRO_0000015640Add
    BLAST
    Propeptidei991 – 9933Removed in mature formSequence AnalysisPRO_0000422293

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei990 – 9901Cysteine methyl esterSequence Analysis
    Lipidationi990 – 9901S-farnesyl cysteineSequence Analysis

    Post-translational modificationi

    Isoprenylation at Cys-990 may be required for localization at the membrane.1 Publication
    May be proteolytically cleaved after Lys-320 as inferred from N-terminal protein sequence of the 75 kda form.1 Publication

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiP32019.
    PaxDbiP32019.
    PRIDEiP32019.

    PTM databases

    PhosphoSiteiP32019.

    Expressioni

    Tissue specificityi

    Platelets.

    Gene expression databases

    ArrayExpressiP32019.
    BgeeiP32019.
    CleanExiHS_INPP5B.
    GenevestigatoriP32019.

    Organism-specific databases

    HPAiHPA028803.

    Interactioni

    Subunit structurei

    Interacts with APPL1, FAM109A and FAM109B. Interacts with several Rab GTPases, at least RAB1A, RAB2A, RAB5A, RAB6A, RAB8A, RAB9A and RAB33B; these interactions may play a dual role in targeting INPP5B to the specific membranes and stimulating the phosphatase activity.4 Publications

    Protein-protein interaction databases

    BioGridi109845. 2 interactions.
    STRINGi9606.ENSP00000362115.

    Structurei

    Secondary structure

    1
    993
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi340 – 35314
    Helixi364 – 3674
    Beta strandi368 – 3703
    Beta strandi375 – 3828
    Helixi388 – 3914
    Helixi397 – 40913
    Beta strandi416 – 4249
    Beta strandi427 – 4348
    Helixi435 – 4406
    Beta strandi441 – 45010
    Helixi453 – 4553
    Beta strandi460 – 46910
    Beta strandi472 – 4809
    Helixi485 – 4873
    Helixi488 – 50114
    Beta strandi509 – 5113
    Beta strandi518 – 52710
    Helixi537 – 5459
    Helixi549 – 5535
    Helixi557 – 5637
    Beta strandi588 – 5914
    Beta strandi604 – 62017
    Beta strandi626 – 6294
    Beta strandi632 – 64312

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MTCX-ray2.40A339-643[»]
    3N9VX-ray2.65A/B342-646[»]
    4CMLX-ray2.30A339-643[»]
    ProteinModelPortaliP32019.
    SMRiP32019. Positions 1-155, 339-643, 656-989.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32019.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 148127PHAdd
    BLAST
    Domaini821 – 993173Rho-GAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni342 – 6683275-phosphataseBy similarityAdd
    BLAST
    Regioni459 – 4602Substrate binding
    Regioni582 – 5832Substrate binding
    Regioni596 – 5983Substrate binding
    Regioni669 – 782114ASHBy similarityAdd
    BLAST

    Domaini

    The ASH (ASPM-SPD2-Hydin) and RhoGAP (Rho GTPase activating) domains form a single folding module. The ASH domain has an immunoglobulin-like fold, the Rho-GAP domain lacks the catalytic arginine and is catalytically inactive. The ASH-RhoGAP module regulates the majority of the protein-protein interactions currently described. The ASH domain mediates association with membrane-targeting Rab GTPases. The Rho-GAP domain interacts with the endocytic adapter APPL1, which is then displaced by FAM109A and FAM109B as endosomes mature, all three interactions relie on F&H motifs, an approximately 12-13 amino-acid sequence centered around Phe and His residues essential for binding By similarity.By similarity

    Sequence similaritiesi

    Contains 1 PH domain.Curated
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5411.
    HOVERGENiHBG000070.
    InParanoidiP32019.
    KOiK01099.
    OMAiPMEIPKE.
    OrthoDBiEOG7J4465.
    PhylomeDBiP32019.
    TreeFamiTF317034.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    3.60.10.10. 1 hit.
    InterProiIPR005135. Endo/exonuclease/phosphatase.
    IPR000300. IPPc.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view]
    PfamiPF03372. Exo_endo_phos. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view]
    SMARTiSM00128. IPPc. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 2 hits.
    SSF56219. SSF56219. 1 hit.
    PROSITEiPS50238. RHOGAP. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P32019-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDQSVAIQET LAEGEYCVIA VQGVLCEGDS RQSRLLGLVR YRLEHGGQEH    50
    ALFLYTHRRM AITGDDVSLD QIVPVSRDFT LEEVSPDGEL YILGSDVTVQ 100
    LDTAELSLVF QLPFGSQTRM FLHEVARACP GFDSATRDPE FLWLSRYRCA 150
    ELELEMPTPR GCNSALVTWP GYATIGGGRY PSRKKRWGLE EARPQGAGSV 200
    LFWGGAMEKT GFRLMERAHG GGFVWGRSAR DGRRDEELEE AGREMSAAAG 250
    SRERNTAGGS NFDGLRPNGK GVPMDQSSRG QDKPESLQPR QNKSKSEITD 300
    MVRSSTITVS DKAHILSMQK FGLRDTIVKS HLLQKEEDYT YIQNFRFFAG 350
    TYNVNGQSPK ECLRLWLSNG IQAPDVYCVG FQELDLSKEA FFFHDTPKEE 400
    EWFKAVSEGL HPDAKYAKVK LIRLVGIMLL LYVKQEHAAY ISEVEAETVG 450
    TGIMGRMGNK GGVAIRFQFH NTSICVVNSH LAAHIEEYER RNQDYKDICS 500
    RMQFCQPDPS LPPLTISNHD VILWLGDLNY RIEELDVEKV KKLIEEKDFQ 550
    MLYAYDQLKI QVAAKTVFEG FTEGELTFQP TYKYDTGSDD WDTSEKCRAP 600
    AWCDRILWKG KNITQLSYQS HMALKTSDHK PVSSVFDIGV RVVNDELYRK 650
    TLEEIVRSLD KMENANIPSV SLSKREFCFQ NVKYMQLKVE SFTIHNGQVP 700
    CHFEFINKPD EESYCKQWLN ANPSRGFLLP DSDVEIDLEL FVNKMTATKL 750
    NSGEDKIEDI LVLHLDRGKD YFLSVSGNYL PSCFGSPIHT LCYMREPILD 800
    LPLETISELT LMPVWTGDDG SQLDSPMEIP KELWMMVDYL YRNAVQQEDL 850
    FQQPGLRSEF EHIRDCLDTG MIDNLSASNH SVAEALLLFL ESLPEPVICY 900
    STYHNCLECS GNYTASKQVI STLPIFHKNV FHYLMAFLRE LLKNSAKNHL 950
    DENILASIFG SLLLRNPAGH QKLDMTEKKK AQEFIHQFLC NPL 993

    Note: No experimental confirmation available.

    Length:993
    Mass (Da):112,852
    Last modified:December 15, 2009 - v4
    Checksum:iABD3581CC6CD29D6
    GO
    Isoform 2 (identifier: P32019-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         178-257: Missing.

    Show »
    Length:913
    Mass (Da):103,987
    Checksum:i4882C26F6E4DC9C6
    GO
    Isoform 3 (identifier: P32019-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-244: Missing.

    Show »
    Length:749
    Mass (Da):85,620
    Checksum:i50921FAACF7E1E39
    GO
    Isoform 4 (identifier: P32019-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         810-828: TLMPVWTGDDGSQLDSPME → LAYLAAYCFETQLVTKSLI
         829-993: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:828
    Mass (Da):93,924
    Checksum:i9CD5C12DCF509A50
    GO

    Sequence cautioni

    The sequence AAA79207.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti587 – 60620GSDDW…WCDRI → RALTTGIPVRSAVLLPGVIG F AA sequence (PubMed:1718960)CuratedAdd
    BLAST
    Sequence conflicti911 – 9111G → P AA sequence (PubMed:1718960)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461G → S.
    Corresponds to variant rs56993041 [ dbSNP | Ensembl ].
    VAR_061270
    Natural varianti745 – 7451M → T.3 Publications
    Corresponds to variant rs11488569 [ dbSNP | Ensembl ].
    VAR_028002

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 244244Missing in isoform 3. CuratedVSP_012821Add
    BLAST
    Alternative sequencei178 – 25780Missing in isoform 2. 1 PublicationVSP_012820Add
    BLAST
    Alternative sequencei810 – 82819TLMPV…DSPME → LAYLAAYCFETQLVTKSLI in isoform 4. 1 PublicationVSP_013902Add
    BLAST
    Alternative sequencei829 – 993165Missing in isoform 4. 1 PublicationVSP_013903Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74161 mRNA. Translation: AAA79207.1. Different initiation.
    AL603790, AL929472 Genomic DNA. Translation: CAH69926.1.
    AL603790, AL929472 Genomic DNA. Translation: CAH69928.1.
    AL603790, AL929472 Genomic DNA. Translation: CAH69929.1.
    AL929472, AL603790 Genomic DNA. Translation: CAH70076.1.
    AL929472, AL603790 Genomic DNA. Translation: CAH70079.1.
    AL929472, AL603790 Genomic DNA. Translation: CAH70080.1.
    BX296560 Genomic DNA. No translation available.
    BC042529 mRNA. Translation: AAH42529.2.
    BC058932 mRNA. Translation: AAH58932.1.
    AL833055 mRNA. Translation: CAH56301.1.
    CCDSiCCDS41306.1. [P32019-2]
    RefSeqiNP_005531.2. NM_005540.2. [P32019-2]
    XP_005270893.1. XM_005270836.1. [P32019-3]
    UniGeneiHs.449942.

    Genome annotation databases

    EnsembliENST00000373023; ENSP00000362114; ENSG00000204084. [P32019-1]
    ENST00000373024; ENSP00000362115; ENSG00000204084. [P32019-2]
    ENST00000373026; ENSP00000362117; ENSG00000204084. [P32019-1]
    ENST00000373027; ENSP00000362118; ENSG00000204084. [P32019-3]
    GeneIDi3633.
    KEGGihsa:3633.
    UCSCiuc001ccf.1. human. [P32019-1]
    uc001ccg.1. human. [P32019-2]

    Polymorphism databases

    DMDMi281185510.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74161 mRNA. Translation: AAA79207.1 . Different initiation.
    AL603790 , AL929472 Genomic DNA. Translation: CAH69926.1 .
    AL603790 , AL929472 Genomic DNA. Translation: CAH69928.1 .
    AL603790 , AL929472 Genomic DNA. Translation: CAH69929.1 .
    AL929472 , AL603790 Genomic DNA. Translation: CAH70076.1 .
    AL929472 , AL603790 Genomic DNA. Translation: CAH70079.1 .
    AL929472 , AL603790 Genomic DNA. Translation: CAH70080.1 .
    BX296560 Genomic DNA. No translation available.
    BC042529 mRNA. Translation: AAH42529.2 .
    BC058932 mRNA. Translation: AAH58932.1 .
    AL833055 mRNA. Translation: CAH56301.1 .
    CCDSi CCDS41306.1. [P32019-2 ]
    RefSeqi NP_005531.2. NM_005540.2. [P32019-2 ]
    XP_005270893.1. XM_005270836.1. [P32019-3 ]
    UniGenei Hs.449942.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MTC X-ray 2.40 A 339-643 [» ]
    3N9V X-ray 2.65 A/B 342-646 [» ]
    4CML X-ray 2.30 A 339-643 [» ]
    ProteinModelPortali P32019.
    SMRi P32019. Positions 1-155, 339-643, 656-989.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109845. 2 interactions.
    STRINGi 9606.ENSP00000362115.

    PTM databases

    PhosphoSitei P32019.

    Polymorphism databases

    DMDMi 281185510.

    Proteomic databases

    MaxQBi P32019.
    PaxDbi P32019.
    PRIDEi P32019.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373023 ; ENSP00000362114 ; ENSG00000204084 . [P32019-1 ]
    ENST00000373024 ; ENSP00000362115 ; ENSG00000204084 . [P32019-2 ]
    ENST00000373026 ; ENSP00000362117 ; ENSG00000204084 . [P32019-1 ]
    ENST00000373027 ; ENSP00000362118 ; ENSG00000204084 . [P32019-3 ]
    GeneIDi 3633.
    KEGGi hsa:3633.
    UCSCi uc001ccf.1. human. [P32019-1 ]
    uc001ccg.1. human. [P32019-2 ]

    Organism-specific databases

    CTDi 3633.
    GeneCardsi GC01M038326.
    HGNCi HGNC:6077. INPP5B.
    HPAi HPA028803.
    MIMi 147264. gene.
    neXtProti NX_P32019.
    PharmGKBi PA29885.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5411.
    HOVERGENi HBG000070.
    InParanoidi P32019.
    KOi K01099.
    OMAi PMEIPKE.
    OrthoDBi EOG7J4465.
    PhylomeDBi P32019.
    TreeFami TF317034.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS05898-MONOMER.
    BRENDAi 3.1.3.36. 2681.
    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
    REACT_150352. Synthesis of IP2, IP, and Ins in the cytosol.
    SABIO-RK P32019.

    Miscellaneous databases

    ChiTaRSi INPP5B. human.
    EvolutionaryTracei P32019.
    GeneWikii INPP5B.
    GenomeRNAii 3633.
    NextBioi 14219.
    PROi P32019.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P32019.
    Bgeei P32019.
    CleanExi HS_INPP5B.
    Genevestigatori P32019.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    3.60.10.10. 1 hit.
    InterProi IPR005135. Endo/exonuclease/phosphatase.
    IPR000300. IPPc.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view ]
    Pfami PF03372. Exo_endo_phos. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view ]
    SMARTi SM00128. IPPc. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 2 hits.
    SSF56219. SSF56219. 1 hit.
    PROSITEi PS50238. RHOGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Properties of type II inositol polyphosphate 5-phosphatase."
      Jefferson A.B., Majerus P.W.
      J. Biol. Chem. 270:9370-9377(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-990, MUTAGENESIS OF CYS-990, VARIANT THR-745.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT THR-745.
      Tissue: Lymph.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-178.
      Tissue: Stomach.
    5. "Cloning and expression of human 75-kDa inositol polyphosphate-5-phosphatase."
      Ross T.S., Jefferson A.B., Mitchell C.A., Majerus P.W.
      J. Biol. Chem. 266:20283-20289(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 284-954, PROTEIN SEQUENCE OF 321-339, VARIANT THR-745.
      Tissue: Placenta.
    6. "Targeting of the type II inositol polyphosphate 5-phosphatase INPP5B to the early secretory pathway."
      Williams C., Choudhury R., McKenzie E., Lowe M.
      J. Cell Sci. 120:3941-3951(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RAB GTPASES.
    7. "Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1."
      Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.
      Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FAM109A.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in the endocytic pathway."
      Noakes C.J., Lee G., Lowe M.
      Mol. Biol. Cell 22:606-623(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FAM109A AND FAM109B.
    10. "Crystal structure of INPP5B in complex with phosphatidylinositol 4-phosphate (CASP target)."
      Structural genomics consortium (SGC)
      Submitted (JUL-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 339-646 IN COMPLEX WITH MAGNESIUM AND PHOSPHATIDYLINOSITOL 4-PHOSPHATE.

    Entry informationi

    Entry nameiI5P2_HUMAN
    AccessioniPrimary (citable) accession number: P32019
    Secondary accession number(s): C9J6U5
    , Q5VSG9, Q5VSH0, Q5VSH1, Q658Q5, Q6P6D4, Q6PD53, Q86YE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: December 15, 2009
    Last modified: October 1, 2014
    This is version 137 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3